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The application of triazine dye affinity chromatography to the large-scale purification of glycerokinase from Bacillus stearothermophilus

✍ Scribed by Michael D. Scawen; Peter M. Hammond; Michael J. Comer; Tony Atkinson

Publisher: Elsevier Science
Year: 1983
Tongue: English
Weight: 362 KB
Volume: 132
Category: Article
ISSN: 0003-2697
DOI: 10.1016/0003-2697(83)90028-3

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✦ Synopsis

Gram quantities of homogeneous glycerokinase have been prepared from the thermophilic bacterium, Bacillus stearothermophilus, using three major steps: precipitation of debris at pH 5.1, ion-exchange chromatography on DEAE-Sephadex, and affinity chromatography on Procion Blue MX-3G-Sepharose. This method is a considerable improvement over conventional techniques; the purified enzyme was obtained with a 40% recovery and a specific activity of 120 units (mumol/min)/mg protein. A modified culture medium enabled yields of 3.4 X 10(6) units of enzyme to be obtained from 400-liter production cultures.

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